Disease relevance of plsB

• In Escherichia coli, acylation of the 1-position of G3P is carried out by PlsB; however, the majority of bacteria lack a plsB gene and in others it is not essential [1].
• We report the initial characterization of a novel gene (termed plsD) from Clostridium butyricum, cloned based on its ability to complement the sn-glycerol-3-phosphate auxotrophic phenotype of a plsB mutant strain of E. coli [2].
• The current findings of embryo death in the homozygous knockout mutant of the plastid LPAAT contrasts with earlier findings of a normal phenotype in the homozygous mutant deficient of the plastid glycerol-3-phosphate acyltransferase; both mutations block the synthesis of plastid phosphatidic acid [3].

High impact information on plsB

• The cessation of phospholipid biosynthesis by the inhibition of the sn-glycerol-3-phosphate acyltransferase using a plsB mutant led to an accumulation of long chain acyl-acyl carrier proteins (acyl-ACP) and the concomitant inhibition of de novo fatty acid biosynthesis in Escherichia coli [4].
• Guanosine tetraphosphate inhibition of fatty acid and phospholipid synthesis in Escherichia coli is relieved by overexpression of glycerol-3-phosphate acyltransferase (plsB) [5].
• Overexpression of the plsB gene product relieved the inhibition of fatty acid and phospholipid synthesis, prevented the accumulation of long-chain acyl-ACPs, and allowed an increase in cell size following elevation of intracellular ppGpp [5].
• Utilization of three hybrid plasmids bearing amber mutations within the plsB gene demonstrated that the 83,000-dalton protein is the sn-glycerol-3-phosphate acyltransferase [6].
• Other experiments have shown that the acyltransferase of a plsB mutant was abnormally thermolabile only when palmitoyl-CoA was the acyl donor in the reaction [7].

Chemical compound and disease context of plsB

• Escherichia coli mutants defective in membrane phospholipid synthesis: binding and metabolism of 1-oleoylglycerol 3-phosphate by a plsB deep rough mutant [8].

Biological context of plsB

• Analysis of Bam HI deletion plasmids demonstrated that a 2.3-megadalton DNA fragment is necessary and sufficient for expression of the plsB gene [6].
• We conclude that GPAT, an inner membrane protein which catalyses the transesterification of a fatty acyl group from acyl coenzyme A or acyl ACP to glycerol-3-phosphate, possesses a binding site for ACP [9].
• Substrate specificity modification of the stromal glycerol-3-phosphate acyltransferase [10].
• Mutagenesis of squash (Cucurbita moschata) glycerol-3-phosphate acyltransferase (GPAT) to produce an enzyme with altered substrate selectivity [11].
• We identified a cDNA containing an open reading frame of 828 amino acids that had an 89% homology with the coding region of the previously characterized mouse mitochondrial GPAT and a predicted amino acid sequence that was 96% identical [12].

Anatomical context of plsB

• These data demonstrate the transmembrane movement of oleoylglycerol-P to the inner surface of the cytoplasmic membrane and suggest that it may become possible to supplement plsB strains of E. coli with acylglycerol-P's [8].

Associations of plsB with chemical compounds

• The size of the plsB polypeptide indicates that a major fraction of the DNA segment to which this gene has been localized is involved in coding for the sn-glycerol-3-phosphate acyltransferase [13].
• Upon glycerol starvation of a plsB- fadE- strain, phospholipid synthesis is 90 percent inhibited [14].
• Neither the catabolic membrane-bound glycerol-3-phosphate dehydrogenase nor the acyl coenzyme A: glycerol-3-phosphate acyltransferase can use 3,4-dihydroxybutyl-1-phosphnate or 2,3-dihydroxypropyl-1-phosphonate are inhibitors of the reduction of dihydroxyactone phosphate as substrates [15].

Analytical, diagnostic and therapeutic context of plsB

• Rat sn-glycerol-3-phosphate acyltransferase: molecular cloning and characterization of the cDNA and expressed protein [12].

References